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PMID: 11331761 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins.

Lougheed JC, Holton JM, Alber T, Bazan JF, Handel TM

Abstract

Melanoma inhibitory activity (MIA) is a 12-kDa protein that is secreted from both chondrocytes and malignant melanoma cells. MIA has been reported to have effects on cell growth and adhesion, and it may play a role in melanoma metastasis and cartilage development. We report the 1.4-A crystal structure of human MIA, which consists of an Src homology 3 (SH3)-like domain with N- and C-terminal extensions of about 20 aa. each. The N- and C-terminal extensions add additional structural elements to the SH3 domain, forming a previously undescribed fold. MIA is a representative of a recently identified family of proteins and is the first structure of a secreted protein with an SH3 subdomain. The structure also suggests a likely protein interaction site and suggests that, unlike conventional SH3 domains, MIA does not recognize polyproline helices.

MeSH Terms
Amino Acid Sequence Extracellular Matrix Proteins Humans Models, Molecular Molecular Sequence Data Neoplasm Proteins/chemistry Protein Conformation Sequence Homology, Amino Acid
Chemicals
Extracellular Matrix Proteins MIA protein, human Neoplasm Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Lougheed J C
Department of Molecular and Cell Biology, 229 Stanley Hall, University of California, Berkeley, CA 94720, USA.
Holton J M
Alber T
Bazan J F
Handel T M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2001-05-08
Epub
2001-00-01
Pages
5515-20
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC33244
Subset
IM
Databases
PDB
Analysis Services
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